75 Integrating Membrane Transport with Male Gametophyte ... - TAIR
75 Integrating Membrane Transport with Male Gametophyte ... - TAIR
75 Integrating Membrane Transport with Male Gametophyte ... - TAIR
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263 Involvement of Cytokinins and Two-Component Elements in Arabidopsis responses to<br />
pathogens<br />
Cristiana Argueso, Joseph Kieber<br />
University of North Carolina at Chapel Hill<br />
Cytokinins are plant hormones involved in many aspects of plant biology and development, such as regulation of cell<br />
division, senescence and sink-source relationships <strong>with</strong>in the plant. While the plant hormones salicylic acid, jasmonic acid<br />
and ethylene have been implicated in the regulation of plant defense responses against pathogens, the role of cytokinins<br />
remains unclear. Recent studies have revealed that cytokinin signaling involves a phosphorelay pathway similar to twocomponent<br />
element response systems, used by bacteria and other organisms to sense and respond to a diverse array of<br />
environmental stimuli. We have tested Arabidopsis mutants <strong>with</strong> T-DNA insertions in genes encoding two-component<br />
elements, as well as transgenic lines, for their susceptibility to biotrophic and necrotrophic pathogens. Some of these<br />
mutants show increased or decreased susceptibility to pathogens, indicating a possible role for two-component elements<br />
and cytokinins in Arabidopsis responses to pathogens. It is possible that cytokinins/ two-component elements could play<br />
a role in plant-pathogen interactions either through the activation of plant defense responses or through the regulation<br />
of sink-source relationships <strong>with</strong>in the plant. Our research may help elucidate additional roles of cytokinins in plant<br />
biology, as well as contribute to a better understanding of plant-pathogen interactions and to the generation of plants<br />
<strong>with</strong> increased disease resistance.<br />
264 Identification of infection-related proteins at the host-pathogen interface of Arabidopsis<br />
Nico Boot 1 , Monique Slijper 2 , Albert Heck 2 , Guido van den Ackerveken 1<br />
1<br />
Molecular Genetics Group, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584<br />
CH Utrecht, The Netherlands, 2 Biomolecular Mass Spectrometry, Department of Chemistry and Department<br />
of Pharmaceutical Sciences, Faculty of Science, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The<br />
Netherlands<br />
The host cell plasma membrane (PM) constitutes an important barrier that restricts extracellular pathogens from<br />
having access to the cytoplasm of the host cell. Being the site of contact between host and pathogen, the PM plays a<br />
key role in nutrient exchange and signal transduction between the interacting organisms. To proliferate extracellularly<br />
pathogens need to suppress host cell defenses and manipulate nutrient metabolism and transport. To achieve this the<br />
bacterial pathogen Pseudomonas syringae pv. tomato (Pst) uses its type III secretion system to inject a plethora of effector<br />
proteins into the host cell cytoplasm. Several of these effectors have been shown to suppress plant defense. However, the<br />
influence of Pst on signaling and transport processes over the PM of the host is unknown. We hypothesize that proteins<br />
involved in these processes are more abundant at the PM during infection. To elucidate the molecular processes occurring<br />
at the host-pathogen interface of Arabidopsis (accession Col-0) <strong>with</strong> virulent Pst (DC3000 strain) we have isolated PM<br />
of mock-treated and Pst-infected Arabidopsis seedlings. Tryptic digests of the PM fractions were subjected to semiquantitative<br />
LC-MS/MS analysis. We have identified several proteins that show differential presence in Pst-infected vs.<br />
mock-treated PM fractions. Our data indicate that several proteins become PM-associated during the infection process<br />
while their overall protein levels do not increase. Functional studies will elucidate if these PM-associated proteins play<br />
an important role during the infection process.